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Immobilization of l-asparaginase on the microparticles of the natural silk sericin protein and its characters

Paper ID Volume ID Publish Year Pages File Format Full-Text
13055 828 2004 9 PDF Available
Title
Immobilization of l-asparaginase on the microparticles of the natural silk sericin protein and its characters
Abstract

The natural silk sericin recovered from Bombyx mori silk waste by the degumming processing in the high-temperature and high-pressure is a macromolecular protein. Amino acid composition and molecular weight range of the sericin protein as a vector for enzyme immobilization were investigated. The silk sericin protein with different molecular mass from 50 to 200 kDa was poorly soluble microparticles with an average size of about 10 μm. Anti-leukemic enzyme l-asparaginase (l-ASNase) was covalently conjugated on the microparticles of the sericin protein. The immobilized l-ASNase on the natural support by cross-linking with glutaraldehyde maintained 62.5% of the original activity of the enzyme. The Km of sericin-conjugates was 8 times lower than that of native l-ASNase. The bioconjugation of l-ASNase widened the optimum reactive temperature range of the enzyme. The immobilized l-ASNase showed significantly higher stability when the temperature raised to 40–50°C, it also showed preferable resistance to trypsin digestion as compared with native enzyme. The results are discussed regarding the possible explanations of sericin-induced enzyme stability, as well as the possible applications of immobilized l-ASNase research.

Keywords
l-Asparaginase; Silk sericin; Immobilization; Microparticle; Stabilization
First Page Preview
Immobilization of l-asparaginase on the microparticles of the natural silk sericin protein and its characters
Publisher
Database: Elsevier - ScienceDirect
Journal: Biomaterials - Volume 25, Issue 17, August 2004, Pages 3751–3759
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering